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Volumn 68, Issue 4, 1997, Pages 1590-1597

Oxidative stress induces dephosphorylation of τ in rat brain primary neuronal cultures

Author keywords

Alzheimer's disease; Excitotoxicity; Free radicals; Neurodegeneration; Reactive oxygen species

Indexed keywords

REACTIVE OXYGEN METABOLITE;

EID: 0030998758     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.68041590.x     Document Type: Article
Times cited : (72)

References (61)
  • 2
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal M. F. (1995) Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 38, 357-366.
    • (1995) Ann. Neurol. , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 3
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C., Davis J. B., Lesley R., and Schubert D. (1994) Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77, 817-828.
    • (1994) Cell , vol.77 , pp. 817-828
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 5
    • 0026048124 scopus 로고
    • The effects of quisqualate and nocodazole on the organization of MAP2 and neurofilaments in spinal cord neurons in vitro
    • Bigot D. and Hunt S. P. (1991) The effects of quisqualate and nocodazole on the organization of MAP2 and neurofilaments in spinal cord neurons in vitro. Neurosci. Lett. 131, 21-26.
    • (1991) Neurosci. Lett. , vol.131 , pp. 21-26
    • Bigot, D.1    Hunt, S.P.2
  • 6
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder L. I., Frankfurter A., and Rebhun L. I. (1985) The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101, 1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 7
    • 0022557147 scopus 로고
    • Differential localization of MAP-2 and tau in mammalian neurons in situ
    • Binder L. I., Frankfurter A., and Rebhun L. I. (1986) Differential localization of MAP-2 and tau in mammalian neurons in situ. Ann. NY Acad. Sci. 466, 145-166.
    • (1986) Ann. NY Acad. Sci. , vol.466 , pp. 145-166
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 8
    • 0000854861 scopus 로고
    • Growth of a neuroblastoma cell line in serum-free supplemented medium
    • Bottenstein J. E. and Sato G. H. (1976) Growth of a neuroblastoma cell line in serum-free supplemented medium. Proc. Natl. Acad. Sci. USA 76, 514-517.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 514-517
    • Bottenstein, J.E.1    Sato, G.H.2
  • 10
    • 0027512745 scopus 로고
    • Neurofilament monoclonal antibodies RT97 and 8D8 recognize different modified epitopes in paired helical filament-τ in Alzheimer's disease
    • Brion J.-P., Couck A.-M., Robertson J., Loviny T. L. F., and Anderton B. H. (1993a) Neurofilament monoclonal antibodies RT97 and 8D8 recognize different modified epitopes in paired helical filament-τ in Alzheimer's disease. J. Neurochem. 60, 1372-1382.
    • (1993) J. Neurochem. , vol.60 , pp. 1372-1382
    • Brion, J.-P.1    Couck, A.-M.2    Robertson, J.3    Loviny, T.L.F.4    Anderton, B.H.5
  • 11
    • 0027429479 scopus 로고
    • Developmental changes in τ phosphorylation: Fetal τ is transiently phosphorylated in a manner similar to paired helical filament-τ characteristic of Alzheimer's disease
    • Brion J.-P., Smith C., Couck A.-M., Gallo J.-M., and Anderton B. H. (1993b) Developmental changes in τ phosphorylation: fetal τ is transiently phosphorylated in a manner similar to paired helical filament-τ characteristic of Alzheimer's disease. J. Neurochem. 61, 2071-2080.
    • (1993) J. Neurochem. , vol.61 , pp. 2071-2080
    • Brion, J.-P.1    Smith, C.2    Couck, A.-M.3    Gallo, J.-M.4    Anderton, B.H.5
  • 12
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering B. M. T. and Coffer P. J. (1995) Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376, 599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.T.1    Coffer, P.J.2
  • 13
    • 0028986916 scopus 로고
    • Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., and Yankner B. A. (1995) β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14, 879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 14
    • 0030071207 scopus 로고    scopus 로고
    • Oxidative stress after acute and chronic application of β-amyloid fragment 25-35 in cortical cultures
    • Café C., Torri C., Bertorelli L., Angeretti N., Lucca E., Forloni G., and Marzatico F. (1996) Oxidative stress after acute and chronic application of β-amyloid fragment 25-35 in cortical cultures. Neurosci. Lett. 203, 61-65.
    • (1996) Neurosci. Lett. , vol.203 , pp. 61-65
    • Café, C.1    Torri, C.2    Bertorelli, L.3    Angeretti, N.4    Lucca, E.5    Forloni, G.6    Marzatico, F.7
  • 15
    • 0026730122 scopus 로고
    • Tyrosine phosphorylation of microtubule-associated protein kinase after transient ischemia in the gerbil brain
    • Campos-González R. and Kindy M. S. (1992) Tyrosine phosphorylation of microtubule-associated protein kinase after transient ischemia in the gerbil brain. J. Neurochem. 59, 1955-1958.
    • (1992) J. Neurochem. , vol.59 , pp. 1955-1958
    • Campos-González, R.1    Kindy, M.S.2
  • 16
    • 0027946642 scopus 로고
    • Oxidative mechanisms involved in kainate-induced cytotoxicity in cortical neurons
    • Cheng Y. and Sun A. Y. (1994) Oxidative mechanisms involved in kainate-induced cytotoxicity in cortical neurons. Neurochem. Res. 19, 1557-1564.
    • (1994) Neurochem. Res. , vol.19 , pp. 1557-1564
    • Cheng, Y.1    Sun, A.Y.2
  • 17
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D. A. E., Alessi D. R., Cohen P., Andjelkovich M., and Hemmings B. A. (1995) Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 18
    • 0029123294 scopus 로고
    • The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures
    • Davis D. R., Brion J.-P., Couck A.-M., Gallo J.-M., Hanger D. P., Ladhani K., Lewis C., Miller C. C. J., Rupniak T., Smith C., and Anderton B. H. (1995) The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures. Biochem. J. 309, 941-949.
    • (1995) Biochem. J. , vol.309 , pp. 941-949
    • Davis, D.R.1    Brion, J.-P.2    Couck, A.-M.3    Gallo, J.-M.4    Hanger, D.P.5    Ladhani, K.6    Lewis, C.7    Miller, C.C.J.8    Rupniak, T.9    Smith, C.10    Anderton, B.H.11
  • 20
    • 0027438048 scopus 로고
    • Activation of p42 mitogen-activated protein kinase by glutamate receptor stimulation in rat primary cortical cultures
    • Fiore R. S., Murphy T. H., Sanghera J. S., Pelech S. L., and Baraban J. M. (1993) Activation of p42 mitogen-activated protein kinase by glutamate receptor stimulation in rat primary cortical cultures. J. Neurochem. 61, 1626-1633.
    • (1993) J. Neurochem. , vol.61 , pp. 1626-1633
    • Fiore, R.S.1    Murphy, T.H.2    Sanghera, J.S.3    Pelech, S.L.4    Baraban, J.M.5
  • 21
    • 0029072567 scopus 로고
    • Modulation of the phosphorylation state of tau in situ: The roles of calcium and cyclic AMP
    • Fleming L. M. and Johnson G. V. W. (1995) Modulation of the phosphorylation state of tau in situ: the roles of calcium and cyclic AMP. Biochem. J. 309, 41-47.
    • (1995) Biochem. J. , vol.309 , pp. 41-47
    • Fleming, L.M.1    Johnson, G.V.W.2
  • 22
    • 0028173238 scopus 로고
    • τ phosphorylation in human, primate, and rat brain: Evidence that a pool of τ is highly phosphorylated in vivo and is rapidly dephosphorylated in vitro
    • Garver T. D., Harris K. A., Lehman R. A. W., Lee V. M.-Y., Trojanowski J. Q., and Billingsley M. L. (1994) τ phosphorylation in human, primate, and rat brain: evidence that a pool of τ is highly phosphorylated in vivo and is rapidly dephosphorylated in vitro. J. Neurochem. 63, 2279-2287.
    • (1994) J. Neurochem. , vol.63 , pp. 2279-2287
    • Garver, T.D.1    Harris, K.A.2    Lehman, R.A.W.3    Lee, V.M.-Y.4    Trojanowski, J.Q.5    Billingsley, M.L.6
  • 23
    • 0028321947 scopus 로고
    • Alterations in τ immunostaining in the rat hippocampus following transient cerebral ischemia
    • Geddes J. W., Schwab C., Craddock S., Wilson J. L., and Pettigrew L. C. (1994) Alterations in τ immunostaining in the rat hippocampus following transient cerebral ischemia. J. Cereb. Blood Flow Metab. 14, 554-564.
    • (1994) J. Cereb. Blood Flow Metab. , vol.14 , pp. 554-564
    • Geddes, J.W.1    Schwab, C.2    Craddock, S.3    Wilson, J.L.4    Pettigrew, L.C.5
  • 24
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert M., Jakes R., Crowther R. A., Cohen P., Vanmechelen E., Vandermeeren M., and Cras P. (1994) Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem. J. 301, 871-877.
    • (1994) Biochem. J. , vol.301 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Cohen, P.4    Vanmechelen, E.5    Vandermeeren, M.6    Cras, P.7
  • 25
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert M., Jakes R., and Vanmechelen E. (1995) Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 189, 167-170.
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-170
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 26
    • 0028856368 scopus 로고
    • NMDA receptor activation produces concurrent generation of nitric oxide and reactive oxygen species: Implication for cell death
    • Gunasekar P. G., Kanthasamy A. G., Borowitz J. L., and Isom G. E. (1995) NMDA receptor activation produces concurrent generation of nitric oxide and reactive oxygen species: implication for cell death. J. Neurochem. 65, 2016-2021.
    • (1995) J. Neurochem. , vol.65 , pp. 2016-2021
    • Gunasekar, P.G.1    Kanthasamy, A.G.2    Borowitz, J.L.3    Isom, G.E.4
  • 27
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger D. P., Hughes K., Woodgett J. R., Brion J.-P., and Anderton B. H. (1992) Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci. Lett. 147, 58-62.
    • (1992) Neurosci. Lett. , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.-P.4    Anderton, B.H.5
  • 28
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons
    • Harris M. E., Hensley K., Butterfield D. A., Leedle R. A., and Carney J. M. (1995) Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons. Exp. Neurol. 131, 193-202.
    • (1995) Exp. Neurol. , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 29
    • 0028353865 scopus 로고
    • Tyrosine phosphorylation and activation of mitogen-activated protein kinase in the rat brain following transient cerebral ischemia
    • Hu B.-R. and Wieloch T. (1994) Tyrosine phosphorylation and activation of mitogen-activated protein kinase in the rat brain following transient cerebral ischemia. J. Neurochem. 62, 1357-1367.
    • (1994) J. Neurochem. , vol.62 , pp. 1357-1367
    • Hu, B.-R.1    Wieloch, T.2
  • 30
    • 0027372016 scopus 로고
    • The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments
    • Kenessey A. and Yen S.-H. C. (1993) The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments. Brain Res. 629, 40-46.
    • (1993) Brain Res. , vol.629 , pp. 40-46
    • Kenessey, A.1    Yen, S.-H.C.2
  • 32
    • 0023690993 scopus 로고
    • Partial sequence of MAP2 in the region of a shared epitope with Alzheimer neurofibrillary tangles
    • Kosik K. S., Orecchio L. D., Bakalis S., Duffy L., and Neve R. L. (1988) Partial sequence of MAP2 in the region of a shared epitope with Alzheimer neurofibrillary tangles. J. Neurochem. 51, 587-598.
    • (1988) J. Neurochem. , vol.51 , pp. 587-598
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Duffy, L.4    Neve, R.L.5
  • 33
    • 0028033159 scopus 로고
    • Changes in the tyrosine phosphorylation of mitogen-activated protein kinase in the rat hippocampus during and following severe hypoglycemia
    • Kurihara J., Hu B.-R., and Wieloch T. (1994) Changes in the tyrosine phosphorylation of mitogen-activated protein kinase in the rat hippocampus during and following severe hypoglycemia. J. Neurochem. 63, 2346-2348.
    • (1994) J. Neurochem. , vol.63 , pp. 2346-2348
    • Kurihara, J.1    Hu, B.-R.2    Wieloch, T.3
  • 34
    • 0029156102 scopus 로고
    • Activation of mitogen-activated protein kinase in cultured rat hippocampal neurons by stimulation of glutamate receptors
    • Kurino M., Fukunaga K., Ushio Y., and Miyamoto E. (1995) Activation of mitogen-activated protein kinase in cultured rat hippocampal neurons by stimulation of glutamate receptors. J. Neurochem. 65, 1282-1289.
    • (1995) J. Neurochem. , vol.65 , pp. 1282-1289
    • Kurino, M.1    Fukunaga, K.2    Ushio, Y.3    Miyamoto, E.4
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0028894984 scopus 로고
    • Disruption of the cytoskeleton in Alzheimer's disease
    • Lee V. M. Y. (1995) Disruption of the cytoskeleton in Alzheimer's disease. Curr. Opin. Neurobiol. 5, 663-668.
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 663-668
    • Lee, V.M.Y.1
  • 39
    • 0028971093 scopus 로고
    • β-Amyloid-induced toxicity in rat hippocampal cells: In vitro evidence for the involvement of free radicals
    • Manelli A. M. and Puttfarcken P. S. (1995) β-Amyloid-induced toxicity in rat hippocampal cells: in vitro evidence for the involvement of free radicals. Brain Res. Bull. 38, 569-576.
    • (1995) Brain Res. Bull. , vol.38 , pp. 569-576
    • Manelli, A.M.1    Puttfarcken, P.S.2
  • 40
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo E. S., Shin R.-W., Billingsley M. L., Van de Voorde A., O'Connor M., Trojanowski J. Q., and Lee V. M.-Y. (1994) Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13, 989-1002.
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.-W.2    Billingsley, M.L.3    Van De Voorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.-Y.7
  • 41
    • 0029162101 scopus 로고
    • Free radicals and disruption of neuronal ion homeostasis in AD: A role for amyloid β-peptide
    • Mattson M. P. (1995a) Free radicals and disruption of neuronal ion homeostasis in AD: a role for amyloid β-peptide. Neurobiol. Aging 16, 679-682.
    • (1995) Neurobiol. Aging , vol.16 , pp. 679-682
    • Mattson, M.P.1
  • 42
    • 0029037264 scopus 로고
    • Degenerative and protective signaling mechanisms in the neurofibrillary pathology of AD
    • Mattson M. P. (1995b) Degenerative and protective signaling mechanisms in the neurofibrillary pathology of AD. Neurobiol. Aging 16, 447-457.
    • (1995) Neurobiol. Aging , vol.16 , pp. 447-457
    • Mattson, M.P.1
  • 43
    • 0028916920 scopus 로고
    • Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium
    • Mattson M. P. and Goodman Y. (1995) Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium. Brain Res. 676, 219-224.
    • (1995) Brain Res. , vol.676 , pp. 219-224
    • Mattson, M.P.1    Goodman, Y.2
  • 44
    • 0028172239 scopus 로고
    • The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases
    • Mawal-Dewan M., Henley J., Van de Voorde A., Trojanowski J. Q., and Lee V. M.-Y. (1994) The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases. J. Biol. Chem. 269, 30981-30987.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30981-30987
    • Mawal-Dewan, M.1    Henley, J.2    Van De Voorde, A.3    Trojanowski, J.Q.4    Lee, V.M.-Y.5
  • 46
    • 0028804835 scopus 로고
    • Glutamate and non-glutamate receptor mediated toxicity caused by oxygen and glucose deprivation in organotypic hippocampal cultures
    • Newell D. W., Barth A., Papermaster V., and Malouf A. T. (1995) Glutamate and non-glutamate receptor mediated toxicity caused by oxygen and glucose deprivation in organotypic hippocampal cultures. J. Neurosci. 15, 7702-7711.
    • (1995) J. Neurosci. , vol.15 , pp. 7702-7711
    • Newell, D.W.1    Barth, A.2    Papermaster, V.3    Malouf, A.T.4
  • 47
    • 0030022901 scopus 로고    scopus 로고
    • Neuronal loss and cytoskeletal disruption following intrahippocampal administration of the metabolic inhibitor malonate: Lack of protection by MK-801
    • Pang Z., Umberger G. H., and Geddes J. W. (1996) Neuronal loss and cytoskeletal disruption following intrahippocampal administration of the metabolic inhibitor malonate: lack of protection by MK-801. J. Neurochem. 66, 474-484.
    • (1996) J. Neurochem. , vol.66 , pp. 474-484
    • Pang, Z.1    Umberger, G.H.2    Geddes, J.W.3
  • 48
    • 0029064518 scopus 로고
    • Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation
    • Reynolds I. J. and Hastings T. G. (1995) Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J. Neurosci. 15, 3318-3327.
    • (1995) J. Neurosci. , vol.15 , pp. 3318-3327
    • Reynolds, I.J.1    Hastings, T.G.2
  • 49
    • 0030030030 scopus 로고    scopus 로고
    • Increased antioxidant enzyme activity in amyloid β protein-resistant cells
    • Sagara Y., Dargusch R., Klier F. G., Schubert D., and Behl C. (1996) Increased antioxidant enzyme activity in amyloid β protein-resistant cells. J. Neurosci. 16, 497-505.
    • (1996) J. Neurosci. , vol.16 , pp. 497-505
    • Sagara, Y.1    Dargusch, R.2    Klier, F.G.3    Schubert, D.4    Behl, C.5
  • 50
    • 0028865376 scopus 로고
    • In situ dephosphorylation of tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons
    • Saito T., Ishiguro K., Uchida T., Miyamoto E., Kishimoto T., and Hisanaga S. (1995) In situ dephosphorylation of tau by protein phosphatase 2A and 2B in fetal rat primary cultured neurons. FEBS Lett. 376, 238-242.
    • (1995) FEBS Lett. , vol.376 , pp. 238-242
    • Saito, T.1    Ishiguro, K.2    Uchida, T.3    Miyamoto, E.4    Kishimoto, T.5    Hisanaga, S.6
  • 53
    • 0030033901 scopus 로고    scopus 로고
    • Changes in phosphorylation of τ during ischemia and reperfusion in the rabbit spinal cord
    • Shackelford D. A. and Nelson K. E. (1996) Changes in phosphorylation of τ during ischemia and reperfusion in the rabbit spinal cord. J. Neurochem. 66, 286-295.
    • (1996) J. Neurochem. , vol.66 , pp. 286-295
    • Shackelford, D.A.1    Nelson, K.E.2
  • 54
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death
    • Shearman M. S., Ragan C. I., and Iversen L. L. (1994) Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death. Proc. Natl. Acad. Sci. USA 91, 1470-1474.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 55
    • 0028000717 scopus 로고
    • Dorothy Russell Memorial Lecture. the molecular pathology of Alzheimer's disease: Are we any closer to understanding the neurodegenerative process?
    • Smith C. and Anderton B. H. (1994) Dorothy Russell Memorial Lecture. The molecular pathology of Alzheimer's disease: are we any closer to understanding the neurodegenerative process? Neuropathol. Appl. Neurobiol. 20, 322-338.
    • (1994) Neuropathol. Appl. Neurobiol. , vol.20 , pp. 322-338
    • Smith, C.1    Anderton, B.H.2
  • 57
    • 0028892186 scopus 로고
    • Amyloid β peptide induces cytoplasmic accumulation of amyloid protein precursor via tau protein kinase I glycogen synthase kinase-3β in rat hippocampal neurons
    • Takashima A., Yamaguchi H., Noguchi K., Michel G., Ishiguro K., Sato K., Hoshino T., Hoshi M., and Imahori K. (1995) Amyloid β peptide induces cytoplasmic accumulation of amyloid protein precursor via tau protein kinase I glycogen synthase kinase-3β in rat hippocampal neurons. Neurosci. Lett. 198, 83-86.
    • (1995) Neurosci. Lett. , vol.198 , pp. 83-86
    • Takashima, A.1    Yamaguchi, H.2    Noguchi, K.3    Michel, G.4    Ishiguro, K.5    Sato, K.6    Hoshino, T.7    Hoshi, M.8    Imahori, K.9
  • 58
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid β peptide (25-35) induces the inactivation of phosphatidylinositol 3-kinase and the activation of tau protein kinase I glycogen synthase kinase-3β
    • Takashima A., Noguchi K., Michel G., Mercken M., Hoshi M., Ishiguro K., and Imahori K. (1996) Exposure of rat hippocampal neurons to amyloid β peptide (25-35) induces the inactivation of phosphatidylinositol 3-kinase and the activation of tau protein kinase I glycogen synthase kinase-3β. Neurosci. Lett. 203, 33-36.
    • (1996) Neurosci. Lett. , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6    Imahori, K.7
  • 60
    • 0029257385 scopus 로고
    • Oxidative stress, age-related neurodegeneration, and the potential for neurotrophic treatment
    • Williams L. R. (1995) Oxidative stress, age-related neurodegeneration, and the potential for neurotrophic treatment. Cerebrovasc. Brain Metab. Rev. 7, 55-73.
    • (1995) Cerebrovasc. Brain Metab. Rev. , vol.7 , pp. 55-73
    • Williams, L.R.1
  • 61
    • 0028868345 scopus 로고
    • Phosphorylated and non-phosphorylated neurofilament proteins: Distribution in the rat hippocampus and early changes after kainic acid induced seizures
    • Yang Q. N., Wang S., Karlsson J. E., Hamberger A., and Haglid K. G. (1995) Phosphorylated and non-phosphorylated neurofilament proteins: distribution in the rat hippocampus and early changes after kainic acid induced seizures. J. Chem. Neuroanat. 9, 217-228.
    • (1995) J. Chem. Neuroanat. , vol.9 , pp. 217-228
    • Yang, Q.N.1    Wang, S.2    Karlsson, J.E.3    Hamberger, A.4    Haglid, K.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.